NIP12_ARATH
ID NIP12_ARATH Reviewed; 294 AA.
AC Q8LFP7; O49406;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Aquaporin NIP1-2;
DE AltName: Full=NOD26-like intrinsic protein 1-2;
DE Short=AtNIP1;2;
DE AltName: Full=Nodulin-26-like major intrinsic protein 2;
DE Short=NodLikeMip2;
DE Short=Protein NLM2;
GN Name=NIP1-2; Synonyms=NLM2; OrderedLocusNames=At4g18910; ORFNames=F13C5.80;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11007982; DOI=10.1016/s0014-5793(00)02027-5;
RA Weig A.R., Jakob C.U.;
RT "Functional identification of the glycerol permease activity of Arabidopsis
RT thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 481:293-298(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=11806824; DOI=10.1186/gb-2001-3-1-research0001;
RA Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.;
RT "From genome to function: the Arabidopsis aquaporins.";
RL Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002).
CC -!- FUNCTION: Water channel probably required to promote glycerol
CC permeability and water transport across cell membranes.
CC {ECO:0000269|PubMed:11007982}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in developing seeds.
CC {ECO:0000269|PubMed:11806824}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala/Gly (NPA).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. NIP (TC
CC 1.A.8.12) subfamily. {ECO:0000305}.
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DR EMBL; AJ250668; CAC14597.1; -; mRNA.
DR EMBL; AL021711; CAA16748.1; -; Genomic_DNA.
DR EMBL; AL161549; CAB78893.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84106.1; -; Genomic_DNA.
DR EMBL; AY072380; AAL62372.1; -; mRNA.
DR EMBL; BT000096; AAN15415.1; -; mRNA.
DR EMBL; AY084720; AAM61294.1; -; mRNA.
DR PIR; T05028; T05028.
DR RefSeq; NP_193626.1; NM_118008.4.
DR AlphaFoldDB; Q8LFP7; -.
DR SMR; Q8LFP7; -.
DR BioGRID; 12919; 1.
DR STRING; 3702.AT4G18910.1; -.
DR TCDB; 1.A.8.12.7; the major intrinsic protein (mip) family.
DR iPTMnet; Q8LFP7; -.
DR PaxDb; Q8LFP7; -.
DR PRIDE; Q8LFP7; -.
DR ProteomicsDB; 250512; -.
DR EnsemblPlants; AT4G18910.1; AT4G18910.1; AT4G18910.
DR GeneID; 827626; -.
DR Gramene; AT4G18910.1; AT4G18910.1; AT4G18910.
DR KEGG; ath:AT4G18910; -.
DR Araport; AT4G18910; -.
DR TAIR; locus:2117184; AT4G18910.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_1_1; -.
DR InParanoid; Q8LFP7; -.
DR OMA; MTRTGMF; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q8LFP7; -.
DR PRO; PR:Q8LFP7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LFP7; baseline and differential.
DR Genevisible; Q8LFP7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0015105; F:arsenite transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0015700; P:arsenite transport; IDA:TAIR.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
DR GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR45724; PTHR45724; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..294
FT /note="Aquaporin NIP1-2"
FT /id="PRO_0000064063"
FT TRANSMEM 54..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 111..113
FT /note="NPA 1"
FT MOTIF 230..232
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT CONFLICT 26
FT /note="Missing (in Ref. 5; AAM61294)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="P -> L (in Ref. 5; AAM61294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 31269 MW; AF337613903285C7 CRC64;
MAEISGNGGD ARDGAVVVNL KEEDEQQQQQ QAIHKPLKKQ DSLLSISVPF LQKLMAEVLG
TYFLIFAGCA AVAVNTQHDK AVTLPGIAIV WGLTVMVLVY SLGHISGAHF NPAVTIAFAS
CGRFPLKQVP AYVISQVIGS TLAAATLRLL FGLDQDVCSG KHDVFVGTLP SGSNLQSFVI
EFIITFYLMF VISGVATDNR AIGELAGLAV GSTVLLNVII AGPVSGASMN PGRSLGPAMV
YSCYRGLWIY IVSPIVGAVS GAWVYNMVRY TDKPLREITK SGSFLKTVRN GSSR
